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Attempts on Parasite Studies
Published in Yamuna Deepani Siriwardana, Leishmaniasis in Sri Lanka, 2023
Controversial evidence has been produced regarding MLEE, and this biochemical technique has been continuously challenged in the recent past by true genetic-based methods. Isoenzyme characterization is a technique introduced in the 1970s (Chance et al., 1974). MLEE examines the enzyme profile of the organism under study and enzyme mobility patterns in an electrically charged field. Organisms within the genus Leishmania are subdivided into species and strains by examining the mobility patterns of a group of iso-enzymes. Parasites are assigned to the main operational taxonomic unit (OTU) known as zymodemes based on the mobility patterns of iso-enzymes. MLEE does not always reflect the true genetic basis of the organism under study (Massamba et al., 1998; Moreno et al., 1986; Cupolillo et al., 1995; Alam et al., 2009; Kuhls et al., 2008). Genetic variation is already known to exist within the Leishmania parasites that belong to the same zymodeme (Reale et al., 2010). Genetic studies on zymodeme MON-37 of L. donovani have not really reflected the genetic or geographical basis of the said classification (Alam et al., 2009).
Evaluation of the Dermal Irritancy of Chemicals
Published in David W. Hobson, Dermal and Ocular Toxicology, 2020
Over 700 enzymes have been isolated, each capable of catalyzing a specific organic or inorganic reaction. Some enzymes are found only in specific organs, while others are found in most every cell of the body. Enzymes may also be quite specific to certain compartments or organelles within the cells, such as cytosol, lysosomes, peroxisomes, membrane border, nucleus or nucleolus, endoplasmic reticulum, Golgi bodies, or mitochondria. Enzymes common to many or most organs of an individual animal may exist in different forms, which demonstrate dissimilar patterns on electrophoresis. Different forms of the same enzyme are called isozymes, or, more preferably, isoenzymes. Levels of enzymes in body fluids usually have a “normal” range which often varies with species, age, sex, etc., and may vary from one individual animal to another. Using blood, one or more baseline levels may be obtained prior to any procedure. Increased levels of enzymes may be due to leakage from injured or dying cells, or due to increased synthesis as a result of damage or tissue insult or an increase in the number or activity of cells producing the enzyme.
The Cardiovascular System and its Disorders
Published in Walter F. Stanaszek, Mary J. Stanaszek, Robert J. Holt, Steven Strauss, Understanding Medical Terms, 2020
Walter F. Stanaszek, Mary J. Stanaszek, Robert J. Holt, Steven Strauss
Laboratory tests utilized to evaluate myocardial damage, such as from a myocardial infarction, include determination of serum creatine phosphokinase (CPK) and lactic dehydrogenase (LDH), both of which are released when muscle is damaged. CPK levels rise within 3-4 hours of an MI, but other muscle damage (such as an IM injection) will also elevate levels of the enzyme: isoenzyme studies can help distinguish the origin of elevated CPK. LDH also rises in response to numerous events, but electrophoresis can separate the isoenzymes to differentiate between myocarditis and congestive heart failure, for example.
Discovery of new pyridine-quinoline hybrids as competitive and non-competitive PIM-1 kinase inhibitors with apoptosis induction and caspase 3/7 activation capabilities
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2023
Mostafa M. M. El-Miligy, Marwa E. Abdelaziz, Salwa M. Fahmy, Tamer M. Ibrahim, Marwa M. Abu-Serie, Mona A. Mahran, Aly A. Hazzaa
Commonly, 50–90% of therapeutic molecules are judged to be a substrate of at least one of the five major isoforms of Cytochrome P (CYP) enzymes (CYP1A2, CYP2C19, CYP2C9, CYP2D6, and CYP3A4)36,42,43. Inhibition of these isoenzymes is unquestionably one cause of pharmacokinetics-related drug-drug interactions leading to toxic or adverse effects44,45. As shown in Table 6, all molecules were predicted to display inhibition of at least one of the CYP isoforms, with exception of 13a. This recommends administering these candidates in a sole regime and not in combination with other therapeutic agents. Fortunately, all molecules showed no alert to be a possible PAINS (pan-assay interference compounds)46, as shown in Table 6. This stresses that their chemical structures would not interfere in protein assays denoting the in-vitro results to be robust with minimum artefacts. Lastly, drug-likeness properties underlined that all molecules do not display violations for the Lipinski and Veber rules47 highlighting that these candidates would demonstrate good bioavailability profiles.
Synthesis, molecular modelling and QSAR study of new N-phenylacetamide-2-oxoindole benzensulfonamide conjugates as carbonic anhydrase inhibitors with antiproliferative activity
Published in Journal of Enzyme Inhibition and Medicinal Chemistry, 2022
Mona F. Said, Riham F. George, Andrea Petreni, Claudiu T. Supuran, Nada M. Mohamed
Human CAs (hCAs) are represented by 15 isoforms which include the cytosolic (I, II, III, VII, XIII), mitochondrial (VA, VB), secreted (VI), and membrane associated (IV, IX, XII, XIV) in addition to the catalytic isoforms of carbonic anhydrase related proteins located in cytosol (VIII, X, XI)5–8. Fluctuation in CA expression levels can lead to hypertension, glaucoma, epilepsy, neuropathic pain, cancer, etc. Accordingly, many hCA isoforms are considered as attractive therapeutic targets for many pharmacological applications9,10. Recently, CA inhibitors (CAIs) were adopted as a combination therapy for solid tumours upon acknowledging the overexpression of the membrane-associated isoenzymes hCA IX and hCA XII in that kind of tumours. Those isoenzymes were discovered to play pivotal role in microenvironment pH regulation thus being important in the survival, proliferation, metastasis and development of drug resistance of malignant cells11,12.
Finasteride for hair loss: a review
Published in Journal of Dermatological Treatment, 2022
A. K. Gupta, M. Venkataraman, M. Talukder, M. A. Bamimore
The enzyme 5AR family (types I, II, and III) participates in bile, androgen, and estrogen metabolism (10). Three distinct 5AR isoenzymes, type I, II, and III are found across mammalian species and influence progesterone, corticosteroid, and androgen metabolism (11,12). The physiological distribution of 5AR isoenzymes is listed in Table 1. The Type I isoform is found predominantly in the liver, sebaceous glands in skin, including scalp, and to a lesser extent in the male reproductive organs such as the prostate; type II is abundantly expressed in the prostate and hair follicles, and to a lesser extent in liver (13–15); while the data on the localization of the type III enzyme is limited, it is expressed in prostate basal epithelial cells (12). Genes for 5AR type I and II were expressed in cultured dermal papilla cells from beard and scalp hair follicles (16). The type I isoenzyme is responsible for about 1/3rd of circulating DTH and the type II is responsible for 2/3rds of circulating DTH (7).